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Updated: May 11, 2026
04:48
A High-throughput Calcium-flux Assay to Study NMDA-receptors with Sensitivity to Glycine/D-serine and Glutamate
Published on: July 10, 2018
Dendritic GluN2A synthesis mediates activity-induced NMDA receptor insertion
Sharon A Swanger1, Yuncen A He, Joel D Richter
1Department of Cell Biology, Emory University School of Medicine, Atlanta, Georgia 30322, USA.
Summary
Dendritic protein synthesis is crucial for activity-induced surface expression of NMDA receptors. This process, regulated by cytoplasmic polyadenylation elements, controls synaptic plasticity in neurons.
Area of Science:
- Neuroscience
- Molecular Biology
- Cell Biology
Background:
- Long-term synaptic plasticity relies on cell-surface protein dynamics.
- mRNA localization to dendrites suggests local protein synthesis, but its necessity for surface expression is unclear.
Purpose of the Study:
- To investigate if dendritic protein synthesis is required for activity-induced surface expression of specific cell-surface proteins.
- To elucidate the regulatory mechanisms controlling NMDA receptor surface expression during synaptic plasticity.
Main Methods:
- Utilized microfluidic devices for precise control and observation in rat hippocampal neurons.
- Visualized activity-induced local translation of GluN2A mRNA and subsequent protein membrane insertion in dendrites.
Main Results:
- Dendritic protein synthesis was demonstrated as essential for activity-induced insertion of GluN2A-containing NMDA receptors.
- Local translation of GluN2A mRNA and its membrane insertion in dendrites were directly observed.
- This process was shown to depend on a 3' untranslated region cytoplasmic polyadenylation element and its translation complex.
Conclusions:
- Dendritic protein synthesis is a critical requirement for NMDA receptor surface expression.
- A novel mechanism involving cytoplasmic polyadenylation element-mediated posttranscriptional regulation of GluN2A mRNA controls NMDA receptor surface expression.
- These findings provide new insights into the molecular basis of synaptic plasticity.
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